ReviewJournal of bioenergetics and biomembranes2007
The roles of the Na,K-ATPase beta 1 subunit in pump sorting and epithelial integrity.
Review in Journal of bioenergetics and biomembranes, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Post-translational modifications of na+/K+-atpase subunits: regulatory mechanisms and functional implications.Frontiers in cell and developmental biology · 2026Review
- Connecting the Dots: AMOG/βInternational journal of molecular sciences · 2025Review
- Na+,K+-ATPase α isoforms in sperm show a highly structured and distinct pattern of distribution.Reproduction (Cambridge, England) · 2025Article
- In silico studies provide new structural insights into trans-dimerization of β1 and β2 subunits of the Na+, K+-ATPase.PloS one · 2025Article
- Na,K-ATPase mediated and cardiotonic induced signaling in health and disease.Frontiers in physiology · 2025Review
- Molecular Basis of Na, K-ATPase Regulation of Diseases: Hormone and FXYD2 Interactions.International journal of molecular sciences · 2024Review
- The βInternational journal of molecular sciences · 2022Article
- Role of NaJournal of molecular medicine (Berlin, Germany) · 2022Review
- Na,K-ATPase Atp1a4 isoform is important for maintaining sperm flagellar shape.Journal of assisted reproduction and genetics · 2021Article
- FXYD proteins and sodium pump regulatory mechanisms.The Journal of general physiology · 2021Review
- NDRG2 Protects the Brain from Excitotoxicity by Facilitating Interstitial Glutamate Uptake.Translational stroke research · 2020Article
- Mineralocorticoids modulate the expression of the β-3 subunit of the NaChannels (Austin, Tex.) · 2017Article
- Expression and potential roles of sodium-potassium ATPase and E-cadherin in human gastric adenocarcinoma.PloS one · 2017Article
- Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart: DISTINCT FUNCTIONAL PROPERTIES AND ISOFORM-SELECTIVE INHIBITORS.The Journal of biological chemistry · 2016Article
- P2C-Type ATPases and Their Regulation.Molecular neurobiology · 2016Review
- Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin.Molecular biology of the cell · 2015Article
- Ouabain-induced alterations of the apical junctional complex involve α1 and β1 Na,K-ATPase downregulation and ERK1/2 activation independent of caveolae in colorectal cancer cells.The Journal of membrane biology · 2014Article
- Regulation of Na,K-ATPase β1-subunit in TGF-β2-mediated epithelial-to-mesenchymal transition in human retinal pigmented epithelial cells.Experimental eye research · 2013Article
- N-myc downstream-regulated gene 2, a novel estrogen-targeted gene, is involved in the regulation of Na+/K+-ATPase.The Journal of biological chemistry · 2011Article
- beta-Subunit overexpression alters the stoicheometry of assembled Na-K-ATPase subunits in MDCK cells.American journal of physiology. Renal physiology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In epithelial MDCK cells, the Na,K-ATPase is co-localized with adherens junctions in all stages of monolayer formation starting from initiation of cell-cell contact. The Na,K-ATPase and adherens junction proteins stay partially co-localized even after internalization due to disruption of intercellular contacts by Ca2+ deprivation. Similar to adherens junction proteins, the Na,K-ATPase is resistant to extraction with non-ionic detergent, suggesting pump association with the cytoskeleton. In contrast, the heterodimer formed by expressed unglycosylated Na,K-ATPase beta 1 subunit and the endogenous alpha 1 subunit is easily dissociated from the adherens junctions and cytoskeleton by detergent extraction. The MDCK cells in which half of the endogenous beta 1 subunits in the lateral membrane are substituted by unglycosylated beta 1 subunits display a slower rate of cell-to-cell contact formation and decreased ability to both spread over the surface and migrate. The lack of N-glycans in the Na,K-ATPase beta 1 subunit results in an impairment of mature cell-cell junctions as detected by an increase in the paracellular permeability of the MDCK cell monolayers and by a decrease in resistance of adherens junction proteins to extraction by a non-ionic detergent. Therefore the N-glycans of the Na,K-ATPase beta 1 subunit are important for retention of the pump at the sites of cell-cell contact. Moreover, they are important for the integrity and stability of cell-cell junctions in mature epithelia. In addition, N-glycans contribute to the formation of cell-cell contacts between surface-attached dispersed cells by mediating lamellipodia formation and stabilizing the newly formed adherens junctions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.